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Superoxide dismutase from venom of the ectoparasitoid Scleroderma guani inhibits melanization of hemolymph
Author(s) -
Liu NaiYong,
Huang JingMei,
Ren XueMin,
Xu ZhiWen,
Yan NaiSheng,
Zhu JiaYing
Publication year - 2018
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21503
Subject(s) - hemolymph , biology , prophenoloxidase , venom , superoxide dismutase , biochemistry , innate immune system , immunology , oxidative stress , immune system
Abstract Superoxide dismutase (SOD) known as an important antioxidative stress protein has been recently found in venoms of several parasitoid wasps. However, its functions and characteristics as a virulent factor remain scarcely described. Here, we report the characterization of two venomous SOD genes ( SguaSOD1 and SguaSOD3 ) from the ectoparasitoid, Scleroderma guani . The metal binding sites, cysteine amino acid positions and signature sequences of the SOD family were conserved within SguaSOD1 and SguaSOD3. Relatively high levels of their transcripts were observed in pupae followed a decrease in early adults, after which they had the highest transcriptions, indicating that their productions would be regulated in venom apparatus. Although the two genes showed lower expression in venom apparatus compared to head and thorax, the enzymatic assay revealed that SOD indeed had activity in venom. Further, we showed that recombinant SguaSOD3 suppressed melanization of host hemolymph, implying that this protein used as a virulent factor uniquely impacts the prophenoloxidase cascade.

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